High-resolution neutron protein crystallography with radically small crystal volumes: application of perdeuteration to human aldose reductase
Acta Cryst. (2005). D61, 1413–1417
Full deuteration of human aldose reductase (MW = 36 kDa) significantly improved the neutron diffraction signal/noise ratio compared with that obtained with hydrogen/deuterium partially exchanged samples. Consequently, a good quality data set (2.2 Å resolution at room temperature) was collected on the LADI diffractometer at the ILL neutron source (France), with a crystal volume (0.15 mm
3) radically smaller than usual for neutron diffraction studies. Deuterium atoms are clearly visible in neutron scattering density maps at 2.2 Å resolution (see proline 13, 2
Fo –
Fc map, 1.5 r.m.s. contour).
I. Hazemann, M. T. Dauvergne, M. P. Blakeley, F. Meilleur, M. Haertlein, A. Van Dorsselaer, A. Mitschler, D. A. A. Myles and A. Podjarny